Journal
FUNGAL BIOLOGY REVIEWS
Volume 27, Issue 2, Pages 43-50Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.fbr.2013.05.002
Keywords
Natural product; Nonribosomal peptide synthetase; Secondary metabolism; Substrate specificity
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Funding
- Hans-Knoll-Institute Jena
- Deutsche Forschungsgemeinschaft (DFG)
- International Leibniz Research School for Microbial Interaction (ILRS Mibintact)
- Jena School for Microbial Communication (JSMC)
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A considerable share of fungal small-molecule natural products is assembled via nonribosomal peptide synthetases (NRPSs). Here, we introduce the readers to two topical aspects which have emerged during work with enzymes of both asco- and basidiomycete origin. First, we highlight the function of non-canonical NRPS-like enzymes which lack the ability to make peptide bonds, and we summarize how they contribute to metabolic diversity. Second, we address the question to what extent substrates of fungal peptide synthetases and related enzymes can be predicted out of their primary sequence. (C) 2013 The British Mycological Society. Published by Elsevier Ltd. All rights reserved.
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